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== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[4puf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._14028S Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PUF FirstGlance]. <br>
<table><tr><td colspan='2'>[[4puf]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Salmonella_enterica_subsp._enterica_serovar_Typhimurium_str._14028S Salmonella enterica subsp. enterica serovar Typhimurium str. 14028S]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4PUF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4PUF FirstGlance]. <br>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4puf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4puf OCA], [https://pdbe.org/4puf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4puf RCSB], [https://www.ebi.ac.uk/pdbsum/4puf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4puf ProSAT]</span></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.296&#8491;</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4puf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4puf OCA], [https://pdbe.org/4puf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4puf RCSB], [https://www.ebi.ac.uk/pdbsum/4puf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4puf ProSAT]</span></td></tr>
</table>
</table>
== Function ==
== Function ==
[https://www.uniprot.org/uniprot/SLRP_SALT1 SLRP_SALT1] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host TXN (Thioredoxin). Leads to significant decrease of thioredoxin activity and increase of host cell death (By similarity).
[https://www.uniprot.org/uniprot/SLRP_SALT1 SLRP_SALT1] Effector proteins function to alter host cell physiology and promote bacterial survival in host tissues. This protein is an E3 ubiquitin ligase that interferes with host's ubiquitination pathway. Can ubiquitinate both ubiquitin and host TXN (Thioredoxin). Leads to significant decrease of thioredoxin activity and increase of host cell death (By similarity).
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Salmonella infections are a leading cause of bacterial foodborne illness in the U.S.A. and the European Union Antimicrobial therapy is often administered to treat the infection, but increasingly isolates are being detected that demonstrate resistance to multiple antibiotics. Salmonella enterica contains two virulence-related T3SS (type III secretion systems): one promotes invasion of the intestine and the other one mediates systemic disease. Both of them secrete the SlrP protein acting as E3 ubiquitin ligase in human host cells where it targets Trx1 (thioredoxin-1). SlrP belongs to the NEL family of bacterial E3 ubiquitin ligases that have been observed in two distinct autoinhibitory conformations. We solved the 3D structure of the SlrP-Trx1 complex and determined the Trx1 ubiquitination site. The description of the substrate-binding mode sheds light on the first step of the activation mechanism of SlrP. Comparison with the available structural data of other NEL effectors allowed us to gain new insights into their autoinhibitory mechanism. We propose a molecular mechanism for the regulation of SlrP in which structural constraints sequestrating the NEL domain would be sequentially released. This work thus constitutes a new milestone in the understanding of how these T3SS effectors influence pathogen virulence. It also provides the fundamental basis for future development of new antimicrobials.
The structure of the Slrp-Trx1 complex sheds light on the autoinhibition mechanism of the type III secretion system effectors of the NEL family.,Zouhir S, Bernal-Bayard J, Cordero-Alba M, Cardenal-Munoz E, Guimaraes B, Lazar N, Ramos-Morales F, Nessler S Biochem J. 2014 Nov 15;464(1):135-44. doi: 10.1042/BJ20140587. PMID:25184225<ref>PMID:25184225</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 4puf" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
*[[Thioredoxin 3D structures|Thioredoxin 3D structures]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
*[[Ubiquitin protein ligase 3D structures|Ubiquitin protein ligase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>

Latest revision as of 12:43, 1 March 2024

Complex between the Salmonella T3SS effector SlrP and its human target thioredoxin-1

4puf, resolution 3.30Å

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